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Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
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Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein
Sophie M Korn1, Julian Von Ehr1,2, Karthikeyan Dhamotharan1
1Institute for Molecular Biosciences, Biomolecular Resonance Center (BMRZ), Goethe University Frankfurt, Max-von-Laue-Str. 7-9, 60438 Frankfurt, Germany.
International Journal of Molecular Sciences
|February 25, 2023
Summary
Scaffold attachment factor B2 (SAFB2) proteins bind DNA and RNA using their SAP and RRM domains. This study reveals their nucleic acid preferences and binding interfaces, offering molecular insights into SAFB2 functions.
Area of Science:
- Molecular biology
- Biochemistry
- Genetics
Background:
- Scaffold attachment factor B (SAFB) proteins are nuclear matrix/scaffold binders involved in DNA repair and RNA processing.
- SAFB proteins are ~100 kDa dual nucleic acid-binding proteins, but their DNA/RNA discrimination mechanisms are unclear.
Purpose of the Study:
- To elucidate the DNA- and RNA-binding functions of the SAFB2 protein's SAP and RRM domains.
- To determine nucleic acid preferences and map binding interfaces at a molecular level.
Main Methods:
- Solution NMR spectroscopy was used to study the SAFB2 SAP and RRM domains.
- Sparse data-derived structures were used to map nucleic acid binding interfaces.
Main Results:
- The functional boundaries of SAFB2 SAP and RRM domains were defined.
- Nucleic acid binding preferences and interfaces were identified.
- SAP domain dynamics and potential dimerization were observed, possibly expanding DNA binding.
Conclusions:
- This study provides the first molecular basis for understanding SAFB2 DNA and RNA binding.
- Findings offer insights into SAFB2's chromatin localization and RNA processing roles.
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